Electrostatic interactions involving the extreme C terminus of nuclear export factor CRM1 modulate its affinity for cargo.

Electrostatic interactions involving the extreme C terminus of nuclear export factor CRM1 modulate its affinity for cargo.

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http://www.wikidata.org/entity/Q38673338
Structural Basis of Targeting the Exportin CRM1 in CancerRan-dependent nuclear export mediators: a structural perspectiveStructural basis for cooperativity of CRM1 export complex formationAtomic basis of CRM1-cargo recognition, release and inhibitionLeukemia-Associated Mutations in Nucleophosmin Alter Recognition by CRM1: Molecular Basis of Aberrant TransportAllosteric control of the exportin CRM1 unraveled by crystal structure analysis.Mechanistic insights from the recent structures of the CRM1 nuclear export complex and its disassembly intermediateXPO1 in B cell hematological malignancies: from recurrent somatic mutations to targeted therapy.A cellular reporter to evaluate CRM1 nuclear export activity: functional analysis of the cancer-related mutant E571K.Enzymatically driven transport: a kinetic theory for nuclear export.Phosphorylation of human chromosome maintenance 1 mediates association with 14-3-3 proteins
P2860

Electrostatic interactions involving the extreme C terminus of nuclear export factor CRM1 modulate its affinity for cargo.

Item
http://www.wikidata.org/entity/Q38673338
description
2011 nî lūn-bûn
@nan
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
2011年论文
@zh
2011年论文
@zh-cn
name
Electrostatic interactions inv ...... dulate its affinity for cargo.
@en
type
label
Electrostatic interactions inv ...... dulate its affinity for cargo.
@en
prefLabel
Electrostatic interactions inv ...... dulate its affinity for cargo.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P932
P356
P1433
P1476
Electrostatic interactions inv ...... dulate its affinity for cargo.
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P50
P577
P698
P932